Structure of PDB 5kli Chain Q Binding Site BS01

Receptor Information
>5kli Chain Q (length=179) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GTRRDFLYYATAGAGAVATGAAVWPLINQMNPSADVQALASIFVDVSSVE
PGVQLTVKFLGKPIFIRRRTEADIELGRSVQLGQLVDTNARNANIDAGAE
ATDQNRTLDEAGEWLVMWGVCTHLGCVPIGGVSGDFGGWFCPCHGSHYDS
AGRIRKGPAPENLPIPLAKFIDETTIQLG
Ligand information
Ligand IDFES
InChIInChI=1S/2Fe.2S
InChIKeyNIXDOXVAJZFRNF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04[Fe]1S[Fe]S1
CACTVS 3.341
OpenEye OEToolkits 1.5.0		S1[Fe]S[Fe]1
FormulaFe2 S2
NameFE2/S2 (INORGANIC) CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain5kli Chain Q Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5kli Hydrogen Bonding to the Substrate Is Not Required for Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III.
Resolution2.996 Å
Binding residue
(original residue number in PDB)		C129 H131 L132 C134 C149 C151 H152 S154
Binding residue
(residue number reindexed from 1)		C121 H123 L124 C126 C141 C143 H144 S146
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H152
Catalytic site (residue number reindexed from 1) H144
Enzyme Commision number 7.1.1.8: quinol--cytochrome-c reductase.
Gene Ontology
Molecular Function
GO:0008121 ubiquinol-cytochrome-c reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5kli, PDBe:5kli, PDBj:5kli
PDBsum5kli
PubMed27758861
UniProtQ02762|UCRI_CERSP Ubiquinol-cytochrome c reductase iron-sulfur subunit (Gene Name=petA)

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